Evidence map›Paper›PMID 30794380›Full record

ArticleAnalytical chemistry2019

Enzymatic Tagging of Glycoproteins on the Cell Surface for Their Global and Site-Specific Analysis with Mass Spectrometry.

Fangxu Sun, Suttipong Suttapitugsakul, Ronghu Wu

Abstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Mapping the cancer surface proteome in search of target antigens for immunotherapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Chemical reporters to study mammalian O-glycosylation.Biochemical Society transactions · 2021
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Proteomics for cancer drug design.Expert review of proteomics · 2019
    Article
  17. Article
  18. Article
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Fangxu SunSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience , Georgia Institute of Technology , Atlanta , Georgia 30332 , United States.
Suttipong SuttapitugsakulSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience , Georgia Institute of Technology , Atlanta , Georgia 30332 , United States.
Ronghu WuSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience , Georgia Institute of Technology , Atlanta , Georgia 30332 , United States.ORCID 0000-0001-9493-9462

Funding

Effective MS-Based Methods for Unraveling Cell Surface Protein InteractionsR01GM118803 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI WU, RONGHU · 2017 to 2024
$2.4M
NIGMS NIH HHS R01 GM118803
6 · The paper itself

Abstract

The cell surface is normally covered with sugars that are bound to lipids or proteins. Surface glycoproteins play critically important roles in many cellular events, including cell-cell communications, cell-matrix interactions, and response to environmental cues. Aberrant protein glycosylation on the cell surface is often a hallmark of human diseases such as cancer and infectious diseases. Global analysis of surface glycoproteins will result in a better understanding of glycoprotein functions and the molecular mechanisms of diseases and the discovery of surface glycoproteins as biomarkers and drug targets. Here, an enzyme is exploited to tag surface glycoproteins, generating a chemical handle for their selective enrichment prior to mass spectrometric (MS) analysis. The enzymatic reaction is very efficient, and the reaction conditions are mild, which are well-suited for surface glycoprotein tagging. For biologically triplicate experiments, on average 953 N-glycosylation sites on 393 surface glycoproteins per experiment were identified in MCF7 cells. Integrating chemical and enzymatic reactions with MS-based proteomics, the current method is highly effective to globally and site-specifically analyze glycoproteins only located on the cell surface. Considering the importance of surface glycoproteins, this method is expected to have extensive applications to advance glycoscience.

Indexed as

Cell MembraneGalactose OxidaseGlycosylationHumansIsotope LabelingMCF-7 CellsMembrane GlycoproteinsProteomicsTandem Mass SpectrometryGalactose OxidaseMembrane Glycoproteins

Identifiers

PMID30794380
PMCPMC6518397

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.